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STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
azoRFmn dependent nadh:quinone oxidoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes (201 aa)    
Predicted Functional Partners:
mdaB
Nadph:quinone oxidoreductase mdab; NADPH-specific quinone reductase. Is most active with quinone derivatives and ferricyanide as electron acceptors. Can use menadione, 1,4-naphthoquinone and 1,4-benzoquinone
  
  
 0.930
ycaK
Putative nad(p)h-dependent oxidoreductase ycak; Belongs to the NAD(P)H dehydrogenase (quinone) family
  
  
 0.897
nfsA
Nitroreductase a, nadph-dependent, fmn-dependent; Catalyzes the reduction of nitroaromatic compounds using NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major oxygen-insensitive nitroreductase in E.coli
      
 0.888
nfsB
Dihydropteridine reductase, nad(p)h-dependent, oxygen-insensitive; Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4- dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species
      
 0.871
chrR
Chromate reductase, nad(p)h dehydrogenase (quinone); Catalyzes the reduction of quinones . Acts by simultaneous two-electron transfer, avoiding formation of highly reactive semiquinone intermediates and producing quinols that promote tolerance of H(2)O(2). Quinone reduction is probably the primary biological role of ChrR (By similarity). Can also reduce toxic chromate to insoluble and less toxic Cr(3+). Catalyzes the transfer of three electrons to Cr(6+) producing Cr(3+) and one electron to molecular oxygen without producing the toxic Cr(5+) species and only producing a minimal amount [...]
  
  
 0.860
kefF
Potassium-efflux system ancillary protein for kefc, glutathione-regulated; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC. Can use a wide range of substrates, including electrophilic quinones, and its function could be to reduce the redox toxicity of electrophilic quinones in parallel with acting as triggers for the KefC efflux system
  
  
 0.747
queG
Epoxyqueuosine reductase; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr)
 
      0.741
yhaK
Bicupin-related protein; Does not have quercetin 2,3-dioxygenase activity
  
  
 0.673
solA
N-methyltryptophan oxidase, fad-binding; Catalyzes the oxidative demethylation of N-methyl-L- tryptophan. Can also use other N-methyl amino acids, including sarcosine, which, however, is a poor substrate
      
 0.649
wrbA
Nad(p)h dehydrogenase (quinone); It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH
      
 0.635
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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